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Ulrich Ermler

Ulrich Ermler

D-Index & Metrics

Chemistry

D-Index
57
Citations
13449
World Ranking
10982
National Ranking
793

Overview

Ulrich Ermler is affiliated with the Max Planck Society in Germany. Their research primarily focuses on biochemistry, genetics, and molecular biology, with significant work also in environmental science. Their contributions extend into several subfields, including molecular biology, materials chemistry, renewable energy and sustainability, environmental engineering, and ecology.

The main topics covered in Ulrich Ermler's work include photosynthetic processes and mechanisms, enzyme structure and function, microbial fuel cells and bioremediation, metal-catalyzed oxygenation mechanisms, metalloenzymes and iron-sulfur proteins, anaerobic digestion and biogas production, and bacterial genetics and biotechnology.

Ulrich Ermler has authored multiple papers published in various scientific venues. Recent publications include:

  • Methanogenesis involves direct hydride transfer from H2 to an organic substrate, 2020, Nature Reviews Chemistry
  • Structural Basis of Hydrogenotrophic Methanogenesis, 2020, Annual Review of Microbiology
  • Functional diversity of prokaryotic HdrA(BC) modules: Role in flavin-based electron bifurcation processes and beyond, 2021, Biochimica et Biophysica Acta (BBA) - Bioenergetics
  • Flavins in the electron bifurcation process, 2021, Archives of Biochemistry and Biophysics
  • Structural and spectroscopic characterization of a HdrA-like subunit from Hyphomicrobium denitrificans, 2020, FEBS Journal

Frequent publication venues for Ulrich Ermler's work include:

  • FEBS Journal
  • Nature Communications
  • Proceedings of the National Academy of Sciences
  • bioRxiv (Cold Spring Harbor Laboratory)
  • Annual Review of Microbiology

Ulrich Ermler collaborates regularly with a group of co-authors. Frequent collaborators include Kanwal Kayastha, Wolfgang Buckel, Ulrike Demmer, Sonja Welsch, and Seigo Shima.

Best Publications

  • Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 A resolution: cofactors and protein-cofactor interactions

    Ulrich Ermler;Günter Fritzsch;Susan K Buchanan;Hartmut Michel

  • Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment

    Christian Ostermeier;Axel Harrenga;Ulrich Ermler;Hartmut Michel

  • Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.

    Ulrich Ermler;Wolfgang Grabarse;Seigo Shima;Marcel Goubeaud

  • The Crystal Structure of [Fe]-Hydrogenase Reveals the Geometry of the Active Site

    Seigo Shima;Oliver Pilak;Sonja Vogt;Michael Schick

  • Anaerobic Microbial Degradation of Hydrocarbons : from Enzymatic Reactions to the Environment

    Ralf Rabus;Matthias Boll;Johann Heider;Rainer U. Meckenstock

  • The Structure of cbb3 Cytochrome Oxidase Provides Insights into Proton Pumping

    Sabine Buschmann;Eberhard Warkentin;Hao Xie;Julian David Langer

  • The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex

    Takeshi Hiromoto;Kenichi Ataka;Oliver Pilak;Sonja Vogt

  • Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons.

    Tobias Weinert;Natacha Olieric;Robert Cheng;Steffen Brünle

  • Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution.

    Ulrich Ermler;Roman A. Siddiqui;Rainer Cramm;Bärbel Friedrich

  • Methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction.

    Tristan Wagner;Jürgen Koch;Ulrich Ermler;Seigo Shima

  • Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation

    Wolfgang Grabarse;Felix Mahlert;Seigo Shima;Rudolf K Thauer

  • On the Mechanism of Biological Methane Formation: Structural Evidence for Conformational Changes in Methyl-Coenzyme M Reductase Upon Substrate Binding

    Wolfgang Grabarse;Felix Mahlert;Evert C. Duin;Marcel Goubeaud

  • Ribosome recycling depends on a mechanistic link between the FeS cluster domain and a conformational switch of the twin-ATPase ABCE1

    Dominik Barthelme;Stephanie Dinkelaker;Sonja Verena Albers;Paola Londei

  • Structure of a methyl-coenzyme M reductase from Black Sea mats that oxidize methane anaerobically

    Seigo Shima;Martin Krueger;Tobias Weinert;Ulrike Demmer

  • The methanogenic CO2 reducing-and-fixing enzyme is bifunctional and contains 46 [4Fe-4S] clusters

    Tristan Wagner;Ulrich Ermler;Seigo Shima;Seigo Shima

  • The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration

    Marco Marcia;Ulrich Ermler;Guohong Peng;Hartmut Michel

  • The crystal structure of an [Fe]-hydrogenase-substrate complex reveals the framework for H2 activation.

    Takeshi Hiromoto;Eberhard Warkentin;Johanna Moll;Ulrich Ermler

  • Insight into the mechanism of biological methanol activation based on the crystal structure of the methanol-cobalamin methyltransferase complex

    Christoph H. Hagemeier;Markus Kr̈er;Rudolf K. Thauer;Eberhard Warkentin

  • A new structure-based classification of sulfide:quinone oxidoreductases

    Marco Marcia;Ulrich Ermler;Guohong Peng;Hartmut Michel

  • Active sites of transition-metal enzymes with a focus on nickel.

    Ulrich Ermler;Wolfgang Grabarse;Seigo Shima;Marcel Goubeaud

Frequent Co-Authors

Seigo Shima
Seigo Shima Max Planck Society
Rudolf K. Thauer
Rudolf K. Thauer Max Planck Society
Hartmut Michel
Hartmut Michel Max Planck Society
Peter M. H. Kroneck
Peter M. H. Kroneck University of Konstanz
Matthias Boll
Matthias Boll University of Freiburg
Wolfgang Buckel
Wolfgang Buckel Philipp University of Marburg
Georg Fuchs
Georg Fuchs University of Freiburg
Günter Fritz
Günter Fritz University of Hohenheim
Xiulan Xie
Xiulan Xie Philipp University of Marburg
Christiane Dahl
Christiane Dahl University of Bonn

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